Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–13 of 13 results
Advanced filters: Author: Guillaume Romet-Lemonne Clear advanced filters
  • Liu et al. show that SPIN90 dimerizes and binds two Arp2/3 complexes to nucleate two bidirectional actin filaments and the dimerization domain is conserved in multicellular animals, suggesting that the mechanism of bidirectional actin filament nucleation is conserved.

    • Tianyang Liu
    • Luyan Cao
    • Carolyn A. Moores
    ResearchOpen Access
    Nature Structural & Molecular Biology
    P: 1-10
  • The cofilin family proteins are actin disassembly factors but the disassembly mechanism is poorly understood. Here authors show that cyclase-associated-protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold and reveal how CAP destabilizes the interface between terminal actin subunits.

    • Tommi Kotila
    • Hugo Wioland
    • Pekka Lappalainen
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-14
  • Formins are a family of protein complexes that accelerate actin filament nucleation and elongation. Jegou et al.show that the formin mDia1 can generate mechanical tension in actin filaments, while conversely, pulling forces applied by viscous drag increase formin elongation activity.

    • Antoine Jégou
    • Marie-France Carlier
    • Guillaume Romet-Lemonne
    Research
    Nature Communications
    Volume: 4, P: 1-7
  • The authors report here the structure-function analysis of highly divergent actin from Leishmania parasite. The study reveals remarkably rapid dynamics of parasite actin as well as the underlying molecular basis, thus providing insight into evolution of the actin cytoskeleton.

    • Tommi Kotila
    • Hugo Wioland
    • Pekka Lappalainen
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-18
  • Cytokinetic abscission relies on the local constriction after cytoskeleton disassembly, but it is not known how the actin filaments are disassembled. Here, the authors show that the redox enzyme MICAL1 is recruited by Rab35 and induces oxidation-mediated depolymerization of actin, which is required to recruit ESCRT-III and complete abscission.

    • Stéphane Frémont
    • Hussein Hammich
    • Arnaud Echard
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-16
  • Formins promote actin filament polymerization and capping protein blocks polymerization; both proteins are thought to exclude each other from barbed ends. Here the authors show that both proteins can simultaneously bind barbed ends in a ternary complex while enhancing each other's dissociation from the barbed end.

    • Shashank Shekhar
    • Mikael Kerleau
    • Marie-France Carlier
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-12
  • Cortical tension is thought to be generated by myosin II, and little is known about the role of actin network properties. Chugh et al. demonstrate that actin cortex thickness, determined by actin filament length, influences cortical tension.

    • Priyamvada Chugh
    • Andrew G. Clark
    • Ewa K. Paluch
    Research
    Nature Cell Biology
    Volume: 19, P: 689-697
  • Proteins containing repeats of the WASP homology 2 (WH2) actin-binding module are multifunctional regulators of actin nucleation and assembly. Now biochemical analyses of VopF from Vibrio cholerae reveal a new regulatory mechanism of actin-filament barbed-end dynamics including enhanced nucleation, uncapping and assisted elongation.

    • Julien Pernier
    • Jozsef Orban
    • Marie-France Carlier
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 1069-1076
  • Cellular deformations are largely driven by contractile forces generated by myosin motors in the submembraneous actin cortex. Here we show that these forces are controlled not simply by cortical myosin levels, but rather by myosins spatial arrangement, specifically the extent of their overlap with cortical actin.

    • Binh An Truong Quang
    • Ruby Peters
    • Ewa K. Paluch
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12
  • Actin cytoskeleton underlies key cellular processes, such as membrane dynamics and cell migration. Despite years of research, how cells regulate actin filament assembly and disassembly to establish dynamic actin structures that fulfil these functions remains an exciting area of study.

    • Pekka Lappalainen
    • Tommi Kotila
    • Guillaume Romet-Lemonne
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 23, P: 836-852